Potential Applications of Immobilizedβ-Galactosidase in Food Processing Industries

Abstract

The enzyme β-galactosidase can be obtained from a wide variety of sources such as microorganisms, plants, and animals. The use of β-galactosidase for the hydrolysis of lactose in milk and whey is one of the promising enzymatic applications in food and dairy processing industries. The enzyme can be used in either soluble or immobilized forms but the soluble enzyme can be used only for batch processes and the immobilized form has the advantage of being used in batch wise as well as in continuous operation. Immobilization has been found to be convenient method to make enzyme thermostable and to prevent the loss of enzyme activity. This review has been focused on the different types of techniques used for the immobilization of β-galactosidase and its potential applications in food industry.

Chemical extraction and optimization of intracellular β-galactosidase production from the bacterium Arthrobacter oxydans using Box-Behnken design of response surface methodology

“…β-Galactosidase is considered to be one of the most important enzymes that is widely used in different industries (PIERRE, 2004;PANESAR et al, 2006). It can be found in different groups of microorganisms, plants, and animals, which differ greatly in their properties and structure (PANESAR et al, 2010). Production of β-galactosidase from plant and animal sources is not commercially signifi cant due to higher cost and less yield.…”

Production of β-galactosidase from streptococcus thermophilus for galactooligosaccharides synthesis

“…Microorganisms offer various advantages over other available sources such as easy handling, higher multiplication rate, and high production yield. As a result of commercial interest in β-galactosidase, a large number of microorganisms have been assessed as potential sources for its production (Panesar et al 2010). S. thermophilus is a promising microorganism for the production of β-galactosidase enzyme, since their β-galactosidase is active at neutral pH and is more heat stable than the widely used Kluyveromyces lactis β-galactosidase .…”

A NEW APPROACH TO EVALUATE IMMOBILIZATION OF β-GALACTOSIDASE ON EUPERGIT®C: STRUCTURAL, KINETIC, AND THERMAL CHARACTERIZATION

“…β-Galactosidase immobilization is an effective process for the successful hydrolysis of lactose in that it can overcome the problems associated with the costs of soluble enzymes. 4 Enzymatic immobilization is a complex process that must be studied in consideration of the different aspects of the enzyme, support, and the interaction between them. Therefore, this work aimed to evaluate β-galactosidase immobilization in Eupergit ® C using a differentiated perspective in addition to the conventional evaluation.…”

“…The cultures were grown on a medium containing 10 g of lactose, 5 g of KH 2 PO 4 , 1.2 g of (NH 4 ) 2 SO 4 , 0.4 g of MgSO 4 .7H 2 O, and 1 g of yeast extract in 1 L of 0.2 mol L −1 potassium phosphate buffer, pH 5.5. 12 The medium was sterilized at 121 °C for 15 min, and lactose was sterilized by filtration.…”

“…Supports used include a wide variety of materials, such as inorganic matrices (silica, porous glass, and celite), polysaccharides (agarose, alginate, chitosan, and cellulose), and synthetic polymers (acrylic resins). [4][5][6] With regard to the immobilization process, the methods and supports that are currently used for β-galactosidase include immobilization on anion exchange resins, cellulose-gelatin carrier systems, DEAE agarose, glyoxyl/epoxy/BrCN groups, glutaraldehyde, polyelectrolyte surfaces, silicon surface, Sepabeads-epoxy supports partially modified with boronate, iminodiacetic acid, metal chelates, and ethylenediamine. These methodologies can improve the stability and reusage of the enzyme.…”